| Literature DB >> 18955816 |
Jung Ho Choi1, Mun-Chual Rho, Seung Woong Lee, Ji Na Choi, Hee Jeong Lee, Kyung Sook Bae, Koanhoi Kim, Young Kook Kim.
Abstract
Acyl-coenzyme A: cholesterol acyltransferase (ACAT) catalyzes cholesterol esterification and plays an important role in the intestinal absorption of cholesterol, hepatic production of lipoproteins, and accumulation of cholesteryl ester within cells. During the course of screening to find ACAT inhibitors from microbial sources, the present authors isolated pyripyropene A from Penicillium griseofulvum F1959. Pyripyropene A, an ACAT2-specific inhibitor, has already been produced from Aspergillus fumigatus. Yet, Aspergillus fumigatus is a pathogen and only produces a limited amount of pyripyropene A, making the isolation of pyripyropene A troublesome. In contrast, Penicillium griseofulvum F1959 was found to produce approximately 28 times more pyripyropene A than Aspergillus fumigatus, plus this report also describes the ideal conditions for the production of pyripyropene A by Penicillium griseofulvum F1959 and its subsequent purification.Entities:
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Year: 2008 PMID: 18955816
Source DB: PubMed Journal: J Microbiol Biotechnol ISSN: 1017-7825 Impact factor: 2.351